4n5x: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4n5x|  PDB=4n5x  |  SCENE=  }}
===Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1===


The entry 4n5x is ON HOLD until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/SCMC1_HUMAN SCMC1_HUMAN]] Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria.<ref>PMID:15123600</ref>  


Authors: Yang, Q., Bruschweiler, S., Chou, J.
==About this Structure==
[[4n5x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N5X OCA].  


Description: Crystal structure of a calmodulin-like protein
==Reference==
<references group="xtra"/><references/>
[[Category: Bruschweiler, S.]]
[[Category: Chou, J.]]
[[Category: Yang, Q.]]
[[Category: Calcium sensor]]
[[Category: Calcium-binding protein]]
[[Category: Calmodulin]]
[[Category: Mitochondrial inner membrane]]

Revision as of 10:41, 18 December 2013

Template:STRUCTURE 4n5x

Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1

Function

[SCMC1_HUMAN] Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria.[1]

About this Structure

4n5x is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  1. ↑ Fiermonte G, De Leonardis F, Todisco S, Palmieri L, Lasorsa FM, Palmieri F. Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution. J Biol Chem. 2004 Jul 16;279(29):30722-30. Epub 2004 Apr 29. PMID:15123600 doi:https://dx.doi.org/10.1074/jbc.M400445200

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